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- PDB-1gng: Glycogen synthase kinase-3 beta (GSK3) complex with FRATtide peptide -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gng | ||||||
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Title | Glycogen synthase kinase-3 beta (GSK3) complex with FRATtide peptide | ||||||
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![]() | TRANSFERASE / PROTEIN KINASE / GSK3-FRATTIDE COMPLEX / PHOSPHORYLATED / ACTIVE | ||||||
Function / homology | ![]() regulation of microtubule anchoring at centrosome / negative regulation of glycogen (starch) synthase activity / neuron projection organization / negative regulation of mesenchymal stem cell differentiation / beta-catenin destruction complex disassembly / negative regulation of type B pancreatic cell development / superior temporal gyrus development / positive regulation of protein localization to cilium / negative regulation of glycogen biosynthetic process / negative regulation of dopaminergic neuron differentiation ...regulation of microtubule anchoring at centrosome / negative regulation of glycogen (starch) synthase activity / neuron projection organization / negative regulation of mesenchymal stem cell differentiation / beta-catenin destruction complex disassembly / negative regulation of type B pancreatic cell development / superior temporal gyrus development / positive regulation of protein localization to cilium / negative regulation of glycogen biosynthetic process / negative regulation of dopaminergic neuron differentiation / maintenance of cell polarity / positive regulation of protein localization to centrosome / : / positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / positive regulation of cilium assembly / negative regulation of protein acetylation / APC truncation mutants have impaired AXIN binding / AXIN missense mutants destabilize the destruction complex / Truncations of AMER1 destabilize the destruction complex / beta-catenin destruction complex / tau-protein kinase / CRMPs in Sema3A signaling / heart valve development / regulation of microtubule-based process / regulation of protein export from nucleus / Beta-catenin phosphorylation cascade / Signaling by GSK3beta mutants / CTNNB1 S33 mutants aren't phosphorylated / CTNNB1 S37 mutants aren't phosphorylated / CTNNB1 S45 mutants aren't phosphorylated / CTNNB1 T41 mutants aren't phosphorylated / Maturation of nucleoprotein / cellular response to interleukin-3 / Wnt signalosome / negative regulation of protein localization to nucleus / negative regulation of TOR signaling / regulation of long-term synaptic potentiation / Disassembly of the destruction complex and recruitment of AXIN to the membrane / Maturation of nucleoprotein / AKT phosphorylates targets in the cytosol / negative regulation of calcineurin-NFAT signaling cascade / positive regulation of cell-matrix adhesion / regulation of axon extension / G protein-coupled dopamine receptor signaling pathway / negative regulation of phosphoprotein phosphatase activity / regulation of dendrite morphogenesis / establishment of cell polarity / regulation of axonogenesis / tau-protein kinase activity / molecular function inhibitor activity / glycogen metabolic process / ER overload response / Constitutive Signaling by AKT1 E17K in Cancer / protein kinase A catalytic subunit binding / dynactin binding / NF-kappaB binding / Regulation of HSF1-mediated heat shock response / epithelial to mesenchymal transition / negative regulation of osteoblast differentiation / canonical Wnt signaling pathway / negative regulation of protein-containing complex assembly / positive regulation of autophagy / regulation of microtubule cytoskeleton organization / regulation of cellular response to heat / cellular response to retinoic acid / extrinsic apoptotic signaling pathway / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / extrinsic apoptotic signaling pathway in absence of ligand / presynaptic modulation of chemical synaptic transmission / negative regulation of insulin receptor signaling pathway / excitatory postsynaptic potential / positive regulation of protein export from nucleus / positive regulation of GTPase activity / positive regulation of protein ubiquitination / Ubiquitin-dependent degradation of Cyclin D / hippocampus development / positive regulation of cell differentiation / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / peptidyl-threonine phosphorylation / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / positive regulation of protein-containing complex assembly / Degradation of beta-catenin by the destruction complex / negative regulation of canonical Wnt signaling pathway / tau protein binding / B-WICH complex positively regulates rRNA expression / regulation of circadian rhythm / beta-catenin binding / circadian rhythm / positive regulation of protein catabolic process / cellular response to amyloid-beta / Regulation of RUNX2 expression and activity / neuron projection development / positive regulation of neuron apoptotic process / p53 binding / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / positive regulation of canonical Wnt signaling pathway / presynapse / positive regulation of protein binding / insulin receptor signaling pathway Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Bax, B. / Carter, P.S. / Lewis, C. / Guy, A.R. / Bridges, A. / Tanner, R. / Pettman, G. / Mannix, C. / Culbert, A.A. / Brown, M.J.B. ...Bax, B. / Carter, P.S. / Lewis, C. / Guy, A.R. / Bridges, A. / Tanner, R. / Pettman, G. / Mannix, C. / Culbert, A.A. / Brown, M.J.B. / Smith, D.G. / Reith, A.D. | ||||||
![]() | ![]() Title: The Structure of Phosphorylated Gsk-3Beta Complexed with a Peptide, Frattide, that Inhibits Beta-Catenin Phosphorylation Authors: Bax, B. / Carter, P.S. / Lewis, C. / Guy, A.R. / Bridges, A. / Tanner, R. / Pettman, G. / Mannix, C. / Culbert, A.A. / Brown, M.J.B. / Smith, D.G. / Reith, A.D. | ||||||
History |
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Remark 285 | THE SPACE-GROUP H 3 2 IS THE HEXAGONAL SETTING OF R 3 2 (NO 155) |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 165.4 KB | Display | ![]() |
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PDB format | ![]() | 130.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 419 KB | Display | ![]() |
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Full document | ![]() | 434.9 KB | Display | |
Data in XML | ![]() | 18.3 KB | Display | |
Data in CIF | ![]() | 27.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2erkS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 43126.277 Da / Num. of mol.: 2 / Fragment: RESIDUES 27-393 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | Mass: 4543.136 Da / Num. of mol.: 2 / Fragment: RESIDUES 188-226 / Source method: obtained synthetically / Source: (synth.) ![]() #3: Chemical | ChemComp-SO4 / #4: Chemical | ChemComp-TRS / | #5: Water | ChemComp-HOH / | Sequence details | NOTE RESIDUE 350 IS LEU (CF HIS IN SWISSPROT) SEE REFERENCE BIOCHEM. J. 303:701-704(1994) | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 50 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: 1.6M AMMONIUM SULPHATE, 0.1M TRIS PH7.5, pH 7.50 | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 277 K / pH: 8.2 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Date: Apr 15, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9326 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→25 Å / Num. obs: 29716 / % possible obs: 100 % / Redundancy: 11.2 % / Biso Wilson estimate: 52.7 Å2 / Rmerge(I) obs: 0.066 |
Reflection shell | Resolution: 2.6→2.64 Å / Redundancy: 11 % / Rmerge(I) obs: 0.448 / Mean I/σ(I) obs: 5 / % possible all: 100 |
Reflection | *PLUS Highest resolution: 2.6 Å / % possible obs: 99.9 % / Num. measured all: 333047 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2ERK Resolution: 2.6→18 Å / Rfactor Rfree error: 0.007 / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 53.5 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.6→18 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.6→2.76 Å / Rfactor Rfree error: 0.021 / Total num. of bins used: 6
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Refinement | *PLUS % reflection Rfree: 5 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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